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Database: PDB
Entry: 3KDN
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HEADER    LYASE                                   23-OCT-09   3KDN              
TITLE     CRYSTAL STRUCTURE OF TYPE III RUBISCO SP4 MUTANT COMPLEXED WITH 2-CABP
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE;                         
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 SYNONYM: RUBISCO;                                                    
COMPND   5 EC: 4.1.1.39;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOCOCCUS KODAKARAENSIS;                     
SOURCE   3 ORGANISM_TAXID: 69014;                                               
SOURCE   4 STRAIN: KOD1;                                                        
SOURCE   5 GENE: RBCL, TK2290;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3)PLYSS;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-21A(+)                                
KEYWDS    RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE, RUBISCO, CARBON      
KEYWDS   2 DIOXIDE FIXATION, LYASE, MAGNESIUM, METAL-BINDING, MONOOXYGENASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.NISHITANI,M.FUJIHASHI,T.DOI,S.YOSHIDA,H.ATOMI,T.IMANAKA,K.MIKI      
REVDAT   2   02-FEB-11 3KDN    1       JRNL                                     
REVDAT   1   06-OCT-10 3KDN    0                                                
JRNL        AUTH   Y.NISHITANI,S.YOSHIDA,M.FUJIHASHI,K.KITAGAWA,T.DOI,H.ATOMI,  
JRNL        AUTH 2 T.IMANAKA,K.MIKI                                             
JRNL        TITL   STRUCTURE-BASED CATALYTIC OPTIMIZATION OF A TYPE III RUBISCO 
JRNL        TITL 2 FROM A HYPERTHERMOPHILE                                      
JRNL        REF    J.BIOL.CHEM.                  V. 285 39339 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20926376                                                     
JRNL        DOI    10.1074/JBC.M110.147587                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.09 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 327701                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 17388                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.09                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.14                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 17951                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 71.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 954                          
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 34127                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 220                                     
REMARK   3   SOLVENT ATOMS            : 2652                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.07000                                              
REMARK   3    B22 (A**2) : -1.66000                                             
REMARK   3    B33 (A**2) : -0.60000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.43000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.208         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.183         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.128         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.808         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 35203 ; 0.004 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 47816 ; 0.768 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4361 ; 4.696 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1607 ;28.021 ;23.441       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5593 ;12.054 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   229 ;17.064 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5093 ; 0.053 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 27095 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 21685 ; 0.294 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 34534 ; 0.562 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13518 ; 0.786 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 13282 ; 1.344 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3KDN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055860.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 345208                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.090                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1GEH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M ACETATE, 80MM CACL2, 6% PEG6000,    
REMARK 280  10% MPD, PH6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      123.12050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 62460 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 125400 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -386.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, B, G, C, F, D, J, E, I          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     PHE A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     PHE B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     LYS C     4                                                      
REMARK 465     PHE C     5                                                      
REMARK 465     ASP C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     LYS D     4                                                      
REMARK 465     PHE D     5                                                      
REMARK 465     ASP D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     MET E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     GLU E     3                                                      
REMARK 465     LYS E     4                                                      
REMARK 465     PHE E     5                                                      
REMARK 465     ASP E     6                                                      
REMARK 465     MET F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     GLU F     3                                                      
REMARK 465     LYS F     4                                                      
REMARK 465     PHE F     5                                                      
REMARK 465     ASP F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     MET G     1                                                      
REMARK 465     VAL G     2                                                      
REMARK 465     GLU G     3                                                      
REMARK 465     LYS G     4                                                      
REMARK 465     PHE G     5                                                      
REMARK 465     ASP G     6                                                      
REMARK 465     THR G     7                                                      
REMARK 465     MET H     1                                                      
REMARK 465     VAL H     2                                                      
REMARK 465     GLU H     3                                                      
REMARK 465     LYS H     4                                                      
REMARK 465     PHE H     5                                                      
REMARK 465     ASP H     6                                                      
REMARK 465     MET I     1                                                      
REMARK 465     VAL I     2                                                      
REMARK 465     GLU I     3                                                      
REMARK 465     LYS I     4                                                      
REMARK 465     PHE I     5                                                      
REMARK 465     ASP I     6                                                      
REMARK 465     THR I     7                                                      
REMARK 465     ILE I     8                                                      
REMARK 465     MET J     1                                                      
REMARK 465     VAL J     2                                                      
REMARK 465     GLU J     3                                                      
REMARK 465     LYS J     4                                                      
REMARK 465     PHE J     5                                                      
REMARK 465     ASP J     6                                                      
REMARK 465     THR J     7                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE A   8    CG1  CG2  CD1                                       
REMARK 470     TYR A   9    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A  10    CG   OD1  OD2                                       
REMARK 470     TYR A  11    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A  15    CG   CD   CE   NZ                                   
REMARK 470     TYR A  17    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A  18    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     GLU A  35    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  58    CG   CD1  CD2                                       
REMARK 470     GLU A  65    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 117    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 148    CG   CD   CE   NZ                                   
REMARK 470     LYS A 153    CG   CD   CE   NZ                                   
REMARK 470     LYS A 175    CG   CD   CE   NZ                                   
REMARK 470     GLU A 203    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 211    CG   CD   CE   NZ                                   
REMARK 470     ASP A 345    CG   OD1  OD2                                       
REMARK 470     GLU A 346    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 376    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 421    CG   CD1  CD2                                       
REMARK 470     GLU A 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 426    CG   CD   CE   NZ                                   
REMARK 470     LYS A 429    CG   CD   CE   NZ                                   
REMARK 470     GLU A 436    CG   CD   OE1  OE2                                  
REMARK 470     ILE B   8    CG1  CG2  CD1                                       
REMARK 470     ASP B  10    CG   OD1  OD2                                       
REMARK 470     GLU B  18    CG   CD   OE1  OE2                                  
REMARK 470     LEU B  58    CG   CD1  CD2                                       
REMARK 470     GLU B 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 153    CG   CD   CE   NZ                                   
REMARK 470     GLU B 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 380    CG   CD   OE1  OE2                                  
REMARK 470     ASP C  10    CG   OD1  OD2                                       
REMARK 470     GLU C  65    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 153    CG   CD   CE   NZ                                   
REMARK 470     LYS C 175    CG   CD   CE   NZ                                   
REMARK 470     LYS C 211    CG   CD   CE   NZ                                   
REMARK 470     GLU C 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 380    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 422    CG   OD1  OD2                                       
REMARK 470     GLU C 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 429    CG   CD   CE   NZ                                   
REMARK 470     GLU C 436    CG   CD   OE1  OE2                                  
REMARK 470     ILE D   8    CG1  CG2  CD1                                       
REMARK 470     ASP D  10    CG   OD1  OD2                                       
REMARK 470     GLU D  18    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  21    CG   CD   CE   NZ                                   
REMARK 470     GLU D  65    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 153    CG   CD   CE   NZ                                   
REMARK 470     GLU D 203    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 429    CG   CD   CE   NZ                                   
REMARK 470     THR E   7    OG1  CG2                                            
REMARK 470     ILE E   8    CG1  CG2  CD1                                       
REMARK 470     LEU E  58    CG   CD1  CD2                                       
REMARK 470     GLU E 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 211    CG   CD   CE   NZ                                   
REMARK 470     GLU E 346    CG   CD   OE1  OE2                                  
REMARK 470     GLN E 376    CG   CD   OE1  NE2                                  
REMARK 470     GLU E 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 426    CG   CD   CE   NZ                                   
REMARK 470     LYS E 429    CG   CD   CE   NZ                                   
REMARK 470     VAL E 441    CG1  CG2                                            
REMARK 470     ILE F   8    CG1  CG2  CD1                                       
REMARK 470     ASP F  10    CG   OD1  OD2                                       
REMARK 470     GLU F  18    CG   CD   OE1  OE2                                  
REMARK 470     LEU F  58    CG   CD1  CD2                                       
REMARK 470     TYR F  59    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU F  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 153    CG   CD   CE   NZ                                   
REMARK 470     GLU F 203    CG   CD   OE1  OE2                                  
REMARK 470     ASN F 218    CG   OD1                                            
REMARK 470     GLU F 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 380    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 429    CG   CD   CE   NZ                                   
REMARK 470     ILE G   8    CG1  CG2  CD1                                       
REMARK 470     ASP G  10    CG   OD1  OD2                                       
REMARK 470     GLU G  18    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 144    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 203    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 380    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 429    CG   CD   CE   NZ                                   
REMARK 470     THR H   7    OG1  CG2                                            
REMARK 470     ILE H   8    CG1  CG2  CD1                                       
REMARK 470     ASP H  10    CG   OD1  OD2                                       
REMARK 470     GLU H  65    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 153    CG   CD   CE   NZ                                   
REMARK 470     LYS H 211    CG   CD   CE   NZ                                   
REMARK 470     ASN H 218    CG   OD1                                            
REMARK 470     GLU H 324    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 326    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 328    CG   OD1  OD2                                       
REMARK 470     GLU H 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 380    CG   CD   OE1  OE2                                  
REMARK 470     GLN H 417    CG   CD   OE1  NE2                                  
REMARK 470     LEU H 421    CG   CD1  CD2                                       
REMARK 470     ASP H 422    CG   OD1  OD2                                       
REMARK 470     GLU H 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 426    CG   CD   CE   NZ                                   
REMARK 470     LYS H 429    CG   CD   CE   NZ                                   
REMARK 470     GLU H 436    CG   CD   OE1  OE2                                  
REMARK 470     VAL H 441    CG1  CG2                                            
REMARK 470     ASP I  10    CG   OD1  OD2                                       
REMARK 470     LEU I  58    CG   CD1  CD2                                       
REMARK 470     GLU I  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU I 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 211    CG   CD   CE   NZ                                   
REMARK 470     GLU I 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU I 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 429    CG   CD   CE   NZ                                   
REMARK 470     ILE J   8    CG1  CG2  CD1                                       
REMARK 470     GLU J 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS J 153    CG   CD   CE   NZ                                   
REMARK 470     GLU J 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU J 380    CG   CD   OE1  OE2                                  
REMARK 470     GLU J 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS J 426    CG   CD   CE   NZ                                   
REMARK 470     LYS J 429    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  14       82.72   -152.62                                   
REMARK 500    ALA A  34     -173.26    -63.04                                   
REMARK 500    SER A  51     -104.05   -150.05                                   
REMARK 500    ASP A  82       16.66   -143.61                                   
REMARK 500    ARG A 117       -9.52    -50.08                                   
REMARK 500    ASP A 154      -56.11   -122.21                                   
REMARK 500    THR A 195     -110.96   -111.13                                   
REMARK 500    ASN A 200       87.08   -161.91                                   
REMARK 500    ALA A 232     -170.22   -176.65                                   
REMARK 500    ALA A 283      128.13    -32.40                                   
REMARK 500    MET A 284      -18.27     94.66                                   
REMARK 500    TYR A 357     -110.99     56.54                                   
REMARK 500    ILE A 359      108.25    -58.53                                   
REMARK 500    ASN A 374       18.05   -149.57                                   
REMARK 500    LYS A 426       10.94    -59.39                                   
REMARK 500    THR A 427       -0.24   -146.42                                   
REMARK 500    HIS A 440       27.52   -140.15                                   
REMARK 500    SER B  51      -94.36   -135.36                                   
REMARK 500    PRO B  60       93.67    -66.13                                   
REMARK 500    ALA B 109       35.94   -144.77                                   
REMARK 500    THR B 195     -107.21   -112.61                                   
REMARK 500    SER B 196       57.90   -140.96                                   
REMARK 500    ASN B 200       85.98   -164.54                                   
REMARK 500    ALA B 232     -178.20   -175.91                                   
REMARK 500    MET B 284      -16.35     96.18                                   
REMARK 500    TYR B 357     -115.89     52.02                                   
REMARK 500    SER C  51      -93.27   -134.04                                   
REMARK 500    THR C 195     -111.41   -114.74                                   
REMARK 500    ASN C 200       85.51   -160.03                                   
REMARK 500    ALA C 232     -170.58   -178.51                                   
REMARK 500    MET C 284      -17.74     95.81                                   
REMARK 500    TYR C 357     -118.97     49.10                                   
REMARK 500    SER D  51     -112.42   -135.10                                   
REMARK 500    PRO D  60       81.49    -66.97                                   
REMARK 500    ALA D 109       35.62   -144.92                                   
REMARK 500    THR D 195     -113.35   -113.65                                   
REMARK 500    ASN D 200       84.71   -159.97                                   
REMARK 500    ALA D 232     -173.21   -172.52                                   
REMARK 500    MET D 284      -19.77     95.85                                   
REMARK 500    TYR D 357     -111.96     53.44                                   
REMARK 500    SER E  51      -90.18   -134.43                                   
REMARK 500    ALA E 109       37.27   -144.14                                   
REMARK 500    ASP E 154      -56.63   -124.56                                   
REMARK 500    THR E 195     -112.25   -114.04                                   
REMARK 500    ASN E 200       80.14   -158.57                                   
REMARK 500    ALA E 232     -171.99   -179.68                                   
REMARK 500    MET E 284      -20.15    100.43                                   
REMARK 500    TYR E 357     -113.17     51.06                                   
REMARK 500    PRO E 420      134.68    -36.24                                   
REMARK 500    ASP F  14       87.72   -150.25                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     101 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX A 189   OQ2                                                    
REMARK 620 2 ASP A 191   OD1  89.1                                              
REMARK 620 3 GLU A 192   OE1  97.9  95.7                                        
REMARK 620 4 CAP A 600   O3   86.7 173.2  90.2                                  
REMARK 620 5 CAP A 600   O2   85.8  96.8 167.0  77.5                            
REMARK 620 6 CAP A 600   O7  157.9  99.1 101.6  83.0  72.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX B 189   OQ2                                                    
REMARK 620 2 ASP B 191   OD1  94.2                                              
REMARK 620 3 GLU B 192   OE1  92.7  78.3                                        
REMARK 620 4 CAP B 600   O3   80.7 171.2  94.6                                  
REMARK 620 5 CAP B 600   O7  169.7  95.5  92.4  90.0                            
REMARK 620 6 CAP B 600   O2   97.9 111.2 165.0  76.9  75.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX C 189   OQ2                                                    
REMARK 620 2 ASP C 191   OD1  88.8                                              
REMARK 620 3 GLU C 192   OE1  89.9  90.5                                        
REMARK 620 4 CAP C 600   O2   93.2 105.9 163.3                                  
REMARK 620 5 CAP C 600   O7  168.4  98.3  99.2  76.0                            
REMARK 620 6 CAP C 600   O3   83.0 171.7  89.6  74.5  89.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX D 189   OQ2                                                    
REMARK 620 2 ASP D 191   OD1  89.2                                              
REMARK 620 3 GLU D 192   OE1  93.2  90.1                                        
REMARK 620 4 CAP D 600   O3   86.1 175.3  89.9                                  
REMARK 620 5 CAP D 600   O2   93.8 102.7 165.5  77.9                            
REMARK 620 6 CAP D 600   O7  168.8  97.3  95.9  87.3  75.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX E 189   OQ2                                                    
REMARK 620 2 ASP E 191   OD1  86.3                                              
REMARK 620 3 GLU E 192   OE1  83.8  83.7                                        
REMARK 620 4 CAP E 600   O3   89.4 171.1  88.1                                  
REMARK 620 5 CAP E 600   O2   96.6 107.5 168.8  80.8                            
REMARK 620 6 CAP E 600   O7  176.9  95.2  99.0  89.5  80.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX F 189   OQ2                                                    
REMARK 620 2 ASP F 191   OD1  85.9                                              
REMARK 620 3 GLU F 192   OE1  88.6  86.5                                        
REMARK 620 4 CAP F 600   O3   86.7 171.6  89.2                                  
REMARK 620 5 CAP F 600   O2   92.0 109.0 164.4  75.3                            
REMARK 620 6 CAP F 600   O7  166.3 100.1 104.0  88.0  74.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX G 189   OQ2                                                    
REMARK 620 2 ASP G 191   OD1  86.2                                              
REMARK 620 3 GLU G 192   OE1  92.4  94.7                                        
REMARK 620 4 CAP G 600   O3   88.2 173.9  83.1                                  
REMARK 620 5 CAP G 600   O7  163.6  96.4 103.5  89.7                            
REMARK 620 6 CAP G 600   O2   86.3 104.0 161.1  78.0  77.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX H 189   OQ2                                                    
REMARK 620 2 GLU H 192   OE1  88.5                                              
REMARK 620 3 CAP H 600   O2  101.6 164.8                                        
REMARK 620 4 CAP H 600   O7  167.4  93.2  74.5                                  
REMARK 620 5 CAP H 600   O3   87.4  90.3  79.0  80.2                            
REMARK 620 6 ASP H 191   OD2 103.2  71.7 116.0  89.2 158.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX I 189   OQ2                                                    
REMARK 620 2 ASP I 191   OD1  89.8                                              
REMARK 620 3 GLU I 192   OE1  92.3  88.4                                        
REMARK 620 4 CAP I 600   O2   97.6 104.6 163.6                                  
REMARK 620 5 CAP I 600   O3   91.2 175.8  87.5  79.3                            
REMARK 620 6 CAP I 600   O7  171.3  95.6  94.7  74.4  83.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG J 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX J 189   OQ2                                                    
REMARK 620 2 ASP J 191   OD2  85.8                                              
REMARK 620 3 GLU J 192   OE1  85.0  86.2                                        
REMARK 620 4 CAP J 600   O3   83.3 166.6  85.1                                  
REMARK 620 5 CAP J 600   O2   90.2 110.7 162.1  77.3                            
REMARK 620 6 CAP J 600   O7  169.1 101.3 103.6  90.6  79.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP I 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP J 600                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GEH   RELATED DB: PDB                                   
REMARK 900 THE APO-FORM ABOUT THE SAME ENZYME                                   
REMARK 900 RELATED ID: 3KBO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3A12   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3A13   RELATED DB: PDB                                   
DBREF  3KDN A    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDN B    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDN C    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDN D    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDN E    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDN F    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDN G    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDN H    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDN I    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDN J    1   444  UNP    O93627   RBL_PYRKO        1    444             
SEQADV 3KDN GLU A  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDN ARG A  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDN ASP A  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDN ILE A  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDN THR A  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDN GLU B  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDN ARG B  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDN ASP B  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDN ILE B  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDN THR B  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDN GLU C  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDN ARG C  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDN ASP C  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDN ILE C  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDN THR C  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDN GLU D  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDN ARG D  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDN ASP D  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDN ILE D  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDN THR D  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDN GLU E  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDN ARG E  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDN ASP E  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDN ILE E  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDN THR E  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDN GLU F  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDN ARG F  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDN ASP F  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDN ILE F  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDN THR F  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDN GLU G  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDN ARG G  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDN ASP G  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDN ILE G  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDN THR G  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDN GLU H  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDN ARG H  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDN ASP H  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDN ILE H  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDN THR H  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDN GLU I  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDN ARG I  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDN ASP I  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDN ILE I  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDN THR I  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDN GLU J  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDN ARG J  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDN ASP J  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDN ILE J  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDN THR J  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQRES   1 A  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 A  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 A  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 A  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 A  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 A  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 A  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 A  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 A  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 A  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 A  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 A  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 A  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 A  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 A  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 A  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 A  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 A  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 A  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 A  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 A  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 A  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 A  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 A  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 A  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 A  444  GLU ARG ASP ILE THR ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 A  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 A  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 A  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 A  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 A  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 A  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 A  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 A  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 A  444  PRO VAL                                                      
SEQRES   1 B  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 B  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 B  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 B  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 B  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 B  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 B  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 B  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 B  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 B  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 B  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 B  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 B  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 B  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 B  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 B  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 B  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 B  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 B  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 B  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 B  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 B  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 B  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 B  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 B  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 B  444  GLU ARG ASP ILE THR ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 B  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 B  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 B  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 B  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 B  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 B  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 B  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 B  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 B  444  PRO VAL                                                      
SEQRES   1 C  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 C  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 C  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 C  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 C  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 C  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 C  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 C  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 C  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 C  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 C  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 C  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 C  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 C  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 C  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 C  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 C  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 C  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 C  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 C  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 C  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 C  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 C  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 C  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 C  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 C  444  GLU ARG ASP ILE THR ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 C  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 C  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 C  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 C  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 C  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 C  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 C  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 C  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 C  444  PRO VAL                                                      
SEQRES   1 D  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 D  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 D  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 D  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 D  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 D  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 D  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 D  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 D  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 D  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 D  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 D  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 D  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 D  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 D  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 D  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 D  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 D  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 D  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 D  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 D  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 D  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 D  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 D  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 D  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 D  444  GLU ARG ASP ILE THR ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 D  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 D  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 D  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 D  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 D  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 D  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 D  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 D  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 D  444  PRO VAL                                                      
SEQRES   1 E  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 E  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 E  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 E  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 E  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 E  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 E  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 E  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 E  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 E  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 E  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 E  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 E  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 E  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 E  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 E  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 E  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 E  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 E  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 E  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 E  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 E  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 E  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 E  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 E  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 E  444  GLU ARG ASP ILE THR ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 E  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 E  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 E  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 E  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 E  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 E  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 E  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 E  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 E  444  PRO VAL                                                      
SEQRES   1 F  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 F  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 F  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 F  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 F  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 F  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 F  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 F  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 F  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 F  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 F  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 F  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 F  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 F  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 F  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 F  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 F  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 F  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 F  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 F  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 F  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 F  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 F  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 F  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 F  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 F  444  GLU ARG ASP ILE THR ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 F  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 F  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 F  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 F  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 F  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 F  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 F  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 F  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 F  444  PRO VAL                                                      
SEQRES   1 G  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 G  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 G  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 G  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 G  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 G  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 G  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 G  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 G  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 G  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 G  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 G  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 G  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 G  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 G  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 G  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 G  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 G  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 G  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 G  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 G  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 G  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 G  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 G  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 G  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 G  444  GLU ARG ASP ILE THR ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 G  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 G  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 G  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 G  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 G  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 G  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 G  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 G  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 G  444  PRO VAL                                                      
SEQRES   1 H  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 H  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 H  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 H  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 H  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 H  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 H  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 H  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 H  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 H  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 H  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 H  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 H  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 H  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 H  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 H  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 H  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 H  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 H  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 H  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 H  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 H  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 H  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 H  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 H  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 H  444  GLU ARG ASP ILE THR ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 H  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 H  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 H  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 H  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 H  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 H  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 H  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 H  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 H  444  PRO VAL                                                      
SEQRES   1 I  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 I  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 I  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 I  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 I  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 I  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 I  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 I  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 I  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 I  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 I  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 I  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 I  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 I  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 I  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 I  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 I  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 I  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 I  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 I  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 I  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 I  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 I  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 I  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 I  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 I  444  GLU ARG ASP ILE THR ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 I  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 I  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 I  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 I  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 I  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 I  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 I  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 I  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 I  444  PRO VAL                                                      
SEQRES   1 J  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 J  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 J  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 J  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 J  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 J  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 J  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 J  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 J  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 J  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 J  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 J  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 J  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 J  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 J  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 J  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 J  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 J  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 J  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 J  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 J  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 J  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 J  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 J  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 J  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 J  444  GLU ARG ASP ILE THR ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 J  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 J  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 J  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 J  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 J  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 J  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 J  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 J  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 J  444  PRO VAL                                                      
MODRES 3KDN KCX A  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDN KCX B  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDN KCX C  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDN KCX D  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDN KCX E  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDN KCX F  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDN KCX G  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDN KCX H  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDN KCX I  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDN KCX J  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    KCX  A 189      12                                                       
HET    KCX  B 189      12                                                       
HET    KCX  C 189      12                                                       
HET    KCX  D 189      12                                                       
HET    KCX  E 189      12                                                       
HET    KCX  F 189      12                                                       
HET    KCX  G 189      12                                                       
HET    KCX  H 189      12                                                       
HET    KCX  I 189      12                                                       
HET    KCX  J 189      12                                                       
HET     MG  A 500       1                                                       
HET    CAP  A 600      21                                                       
HET     MG  B 500       1                                                       
HET    CAP  B 600      21                                                       
HET     MG  C 500       1                                                       
HET    CAP  C 600      21                                                       
HET     MG  D 500       1                                                       
HET    CAP  D 600      21                                                       
HET     MG  E 500       1                                                       
HET    CAP  E 600      21                                                       
HET     MG  F 500       1                                                       
HET    CAP  F 600      21                                                       
HET     MG  G 500       1                                                       
HET    CAP  G 600      21                                                       
HET     MG  H 500       1                                                       
HET    CAP  H 600      21                                                       
HET     MG  I 500       1                                                       
HET    CAP  I 600      21                                                       
HET     MG  J 500       1                                                       
HET    CAP  J 600      21                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                              
FORMUL   1  KCX    10(C7 H14 N2 O4)                                             
FORMUL  11   MG    10(MG 2+)                                                    
FORMUL  12  CAP    10(C6 H14 O13 P2)                                            
FORMUL  31  HOH   *2652(H2 O)                                                   
HELIX    1   1 TYR A    9  VAL A   13  5                                   5    
HELIX    2   2 THR A   38  SER A   50  1                                  13    
HELIX    3   3 GLU A   63  SER A   71  1                                   9    
HELIX    4   4 HIS A   94  PHE A   96  5                                   3    
HELIX    5   5 ASN A  100  ALA A  109  1                                  10    
HELIX    6   6 GLY A  110  MET A  115  5                                   6    
HELIX    7   7 PRO A  129  ARG A  134  1                                   6    
HELIX    8   8 PHE A  141  GLU A  151  1                                  11    
HELIX    9   9 SER A  169  ASN A  183  1                                  15    
HELIX   10  10 ARG A  201  GLY A  221  1                                  21    
HELIX   11  11 ASP A  233  GLY A  248  1                                  16    
HELIX   12  12 VAL A  256  GLY A  260  1                                   5    
HELIX   13  13 GLY A  260  GLY A  275  1                                  16    
HELIX   14  14 HIS A  285  ARG A  290  1                                   6    
HELIX   15  15 SER A  297  GLY A  309  1                                  13    
HELIX   16  16 GLU A  326  GLU A  339  1                                  14    
HELIX   17  17 ILE A  375  GLY A  383  1                                   9    
HELIX   18  18 GLY A  391  GLY A  396  1                                   6    
HELIX   19  19 GLY A  400  MET A  416  1                                  17    
HELIX   20  20 PRO A  420  LYS A  426  1                                   7    
HELIX   21  21 HIS A  428  GLY A  439  1                                  12    
HELIX   22  22 ILE B    8  VAL B   13  5                                   6    
HELIX   23  23 THR B   38  SER B   50  1                                  13    
HELIX   24  24 GLU B   63  SER B   71  1                                   9    
HELIX   25  25 HIS B   94  PHE B   96  5                                   3    
HELIX   26  26 ASN B  100  ALA B  109  1                                  10    
HELIX   27  27 GLY B  110  MET B  115  5                                   6    
HELIX   28  28 PRO B  129  ARG B  134  1                                   6    
HELIX   29  29 PHE B  141  GLU B  151  1                                  11    
HELIX   30  30 SER B  169  ASN B  183  1                                  15    
HELIX   31  31 ARG B  201  GLY B  221  1                                  21    
HELIX   32  32 ASP B  233  LEU B  247  1                                  15    
HELIX   33  33 VAL B  256  GLY B  260  1                                   5    
HELIX   34  34 GLY B  260  TYR B  274  1                                  15    
HELIX   35  35 HIS B  285  ARG B  290  1                                   6    
HELIX   36  36 SER B  297  GLY B  309  1                                  13    
HELIX   37  37 GLU B  326  GLU B  339  1                                  14    
HELIX   38  38 ILE B  375  GLY B  383  1                                   9    
HELIX   39  39 GLY B  391  GLY B  396  1                                   6    
HELIX   40  40 GLY B  400  GLY B  418  1                                  19    
HELIX   41  41 PRO B  420  ALA B  425  1                                   6    
HELIX   42  42 HIS B  428  GLY B  439  1                                  12    
HELIX   43  43 ILE C    8  VAL C   13  5                                   6    
HELIX   44  44 THR C   38  SER C   50  1                                  13    
HELIX   45  45 GLU C   63  LEU C   70  1                                   8    
HELIX   46  46 HIS C   94  PHE C   96  5                                   3    
HELIX   47  47 ASN C  100  ALA C  109  1                                  10    
HELIX   48  48 GLY C  110  MET C  115  5                                   6    
HELIX   49  49 PRO C  129  ARG C  134  1                                   6    
HELIX   50  50 PHE C  141  GLU C  151  1                                  11    
HELIX   51  51 SER C  169  ASN C  183  1                                  15    
HELIX   52  52 ARG C  201  GLY C  221  1                                  21    
HELIX   53  53 ASP C  233  GLY C  248  1                                  16    
HELIX   54  54 VAL C  256  GLY C  260  1                                   5    
HELIX   55  55 GLY C  260  TYR C  274  1                                  15    
HELIX   56  56 HIS C  285  ARG C  290  1                                   6    
HELIX   57  57 SER C  297  GLY C  309  1                                  13    
HELIX   58  58 GLU C  326  GLU C  339  1                                  14    
HELIX   59  59 HIS C  371  ASN C  374  5                                   4    
HELIX   60  60 ILE C  375  GLY C  383  1                                   9    
HELIX   61  61 GLY C  391  GLY C  396  1                                   6    
HELIX   62  62 GLY C  400  GLN C  417  1                                  18    
HELIX   63  63 PRO C  420  LYS C  426  1                                   7    
HELIX   64  64 HIS C  428  GLY C  439  1                                  12    
HELIX   65  65 TYR D    9  VAL D   13  5                                   5    
HELIX   66  66 THR D   38  SER D   50  1                                  13    
HELIX   67  67 GLU D   63  SER D   71  1                                   9    
HELIX   68  68 HIS D   94  PHE D   96  5                                   3    
HELIX   69  69 ASN D  100  ALA D  109  1                                  10    
HELIX   70  70 GLY D  110  MET D  115  5                                   6    
HELIX   71  71 PRO D  129  ARG D  134  1                                   6    
HELIX   72  72 PHE D  141  GLU D  151  1                                  11    
HELIX   73  73 SER D  169  ASN D  183  1                                  15    
HELIX   74  74 ARG D  201  GLY D  221  1                                  21    
HELIX   75  75 ASP D  233  GLY D  248  1                                  16    
HELIX   76  76 VAL D  256  GLY D  260  1                                   5    
HELIX   77  77 GLY D  260  TYR D  274  1                                  15    
HELIX   78  78 HIS D  285  ARG D  290  1                                   6    
HELIX   79  79 SER D  297  GLY D  309  1                                  13    
HELIX   80  80 GLU D  326  GLU D  339  1                                  14    
HELIX   81  81 HIS D  371  ASN D  374  5                                   4    
HELIX   82  82 ILE D  375  GLY D  383  1                                   9    
HELIX   83  83 GLY D  391  GLY D  396  1                                   6    
HELIX   84  84 GLY D  400  GLY D  418  1                                  19    
HELIX   85  85 PRO D  420  ALA D  425  1                                   6    
HELIX   86  86 HIS D  428  GLY D  439  1                                  12    
HELIX   87  87 ILE E    8  VAL E   13  5                                   6    
HELIX   88  88 THR E   38  SER E   50  1                                  13    
HELIX   89  89 GLU E   63  SER E   71  1                                   9    
HELIX   90  90 HIS E   94  PHE E   96  5                                   3    
HELIX   91  91 ASN E  100  ALA E  109  1                                  10    
HELIX   92  92 GLY E  110  MET E  115  5                                   6    
HELIX   93  93 PRO E  129  ARG E  134  1                                   6    
HELIX   94  94 PHE E  141  GLU E  151  1                                  11    
HELIX   95  95 SER E  169  ASN E  183  1                                  15    
HELIX   96  96 ARG E  201  GLY E  221  1                                  21    
HELIX   97  97 ASP E  233  LEU E  247  1                                  15    
HELIX   98  98 VAL E  256  GLY E  260  1                                   5    
HELIX   99  99 GLY E  260  GLY E  275  1                                  16    
HELIX  100 100 HIS E  285  ARG E  290  1                                   6    
HELIX  101 101 SER E  297  GLY E  309  1                                  13    
HELIX  102 102 GLU E  326  GLU E  339  1                                  14    
HELIX  103 103 ASN E  374  GLY E  383  1                                  10    
HELIX  104 104 GLY E  391  GLY E  396  1                                   6    
HELIX  105 105 GLY E  400  GLN E  417  1                                  18    
HELIX  106 106 PRO E  420  LYS E  426  1                                   7    
HELIX  107 107 HIS E  428  GLY E  439  1                                  12    
HELIX  108 108 TYR F    9  VAL F   13  5                                   5    
HELIX  109 109 THR F   38  SER F   50  1                                  13    
HELIX  110 110 GLU F   63  LEU F   70  1                                   8    
HELIX  111 111 HIS F   94  PHE F   96  5                                   3    
HELIX  112 112 ASN F  100  ALA F  109  1                                  10    
HELIX  113 113 GLY F  110  MET F  115  5                                   6    
HELIX  114 114 PRO F  129  ARG F  134  1                                   6    
HELIX  115 115 PHE F  141  GLU F  151  1                                  11    
HELIX  116 116 SER F  169  ASN F  183  1                                  15    
HELIX  117 117 ARG F  201  GLY F  221  1                                  21    
HELIX  118 118 ASP F  233  LEU F  247  1                                  15    
HELIX  119 119 VAL F  256  GLY F  260  1                                   5    
HELIX  120 120 GLY F  260  TYR F  274  1                                  15    
HELIX  121 121 HIS F  285  ARG F  290  1                                   6    
HELIX  122 122 SER F  297  GLY F  309  1                                  13    
HELIX  123 123 GLU F  326  GLU F  339  1                                  14    
HELIX  124 124 HIS F  371  ASN F  374  5                                   4    
HELIX  125 125 ILE F  375  GLY F  383  1                                   9    
HELIX  126 126 GLY F  391  GLY F  396  1                                   6    
HELIX  127 127 GLY F  400  GLN F  417  1                                  18    
HELIX  128 128 PRO F  420  LYS F  426  1                                   7    
HELIX  129 129 HIS F  428  GLY F  439  1                                  12    
HELIX  130 130 ILE G    8  VAL G   13  5                                   6    
HELIX  131 131 THR G   38  SER G   50  1                                  13    
HELIX  132 132 GLU G   63  SER G   71  1                                   9    
HELIX  133 133 HIS G   94  PHE G   96  5                                   3    
HELIX  134 134 ASN G  100  ALA G  109  1                                  10    
HELIX  135 135 GLY G  110  MET G  115  5                                   6    
HELIX  136 136 PRO G  129  ARG G  134  1                                   6    
HELIX  137 137 PHE G  141  GLU G  151  1                                  11    
HELIX  138 138 SER G  169  ASN G  183  1                                  15    
HELIX  139 139 ARG G  201  GLY G  221  1                                  21    
HELIX  140 140 ASP G  233  LEU G  247  1                                  15    
HELIX  141 141 VAL G  256  GLY G  260  1                                   5    
HELIX  142 142 GLY G  260  TYR G  274  1                                  15    
HELIX  143 143 HIS G  285  ARG G  290  1                                   6    
HELIX  144 144 SER G  297  GLY G  309  1                                  13    
HELIX  145 145 GLU G  326  GLU G  339  1                                  14    
HELIX  146 146 HIS G  371  ASN G  374  5                                   4    
HELIX  147 147 ILE G  375  GLY G  383  1                                   9    
HELIX  148 148 GLY G  391  GLY G  396  1                                   6    
HELIX  149 149 GLY G  400  GLY G  418  1                                  19    
HELIX  150 150 PRO G  420  ALA G  425  1                                   6    
HELIX  151 151 HIS G  428  GLY G  439  1                                  12    
HELIX  152 152 THR H    7  VAL H   13  5                                   7    
HELIX  153 153 THR H   38  SER H   50  1                                  13    
HELIX  154 154 GLU H   63  SER H   71  1                                   9    
HELIX  155 155 HIS H   94  PHE H   96  5                                   3    
HELIX  156 156 ASN H  100  ALA H  109  1                                  10    
HELIX  157 157 GLY H  110  MET H  115  5                                   6    
HELIX  158 158 PRO H  129  ARG H  134  1                                   6    
HELIX  159 159 PHE H  141  GLU H  151  1                                  11    
HELIX  160 160 SER H  169  ASN H  183  1                                  15    
HELIX  161 161 ARG H  201  GLY H  221  1                                  21    
HELIX  162 162 ASP H  233  LEU H  247  1                                  15    
HELIX  163 163 VAL H  256  GLY H  260  1                                   5    
HELIX  164 164 GLY H  260  TYR H  274  1                                  15    
HELIX  165 165 HIS H  285  ARG H  290  1                                   6    
HELIX  166 166 SER H  297  GLY H  309  1                                  13    
HELIX  167 167 GLU H  326  GLU H  339  1                                  14    
HELIX  168 168 ILE H  375  GLY H  383  1                                   9    
HELIX  169 169 GLY H  391  GLY H  396  1                                   6    
HELIX  170 170 GLY H  400  GLN H  417  1                                  18    
HELIX  171 171 PRO H  420  LYS H  426  1                                   7    
HELIX  172 172 HIS H  428  GLY H  439  1                                  12    
HELIX  173 173 TYR I    9  VAL I   13  5                                   5    
HELIX  174 174 THR I   38  SER I   50  1                                  13    
HELIX  175 175 GLU I   63  SER I   71  1                                   9    
HELIX  176 176 HIS I   94  PHE I   96  5                                   3    
HELIX  177 177 ASN I  100  ALA I  109  1                                  10    
HELIX  178 178 GLY I  110  MET I  115  5                                   6    
HELIX  179 179 PRO I  129  ARG I  134  1                                   6    
HELIX  180 180 PHE I  141  GLU I  151  1                                  11    
HELIX  181 181 SER I  169  ASN I  183  1                                  15    
HELIX  182 182 ARG I  201  GLY I  221  1                                  21    
HELIX  183 183 ASP I  233  GLY I  248  1                                  16    
HELIX  184 184 VAL I  256  GLY I  260  1                                   5    
HELIX  185 185 GLY I  260  TYR I  274  1                                  15    
HELIX  186 186 HIS I  285  ARG I  290  1                                   6    
HELIX  187 187 SER I  297  GLY I  309  1                                  13    
HELIX  188 188 GLU I  326  GLU I  339  1                                  14    
HELIX  189 189 HIS I  371  ASN I  374  5                                   4    
HELIX  190 190 ILE I  375  GLY I  383  1                                   9    
HELIX  191 191 GLY I  391  GLY I  396  1                                   6    
HELIX  192 192 GLY I  400  GLY I  418  1                                  19    
HELIX  193 193 PRO I  420  ALA I  425  1                                   6    
HELIX  194 194 HIS I  428  GLY I  439  1                                  12    
HELIX  195 195 ILE J    8  VAL J   13  5                                   6    
HELIX  196 196 THR J   38  SER J   50  1                                  13    
HELIX  197 197 GLU J   63  SER J   71  1                                   9    
HELIX  198 198 HIS J   94  PHE J   96  5                                   3    
HELIX  199 199 ASN J  100  ALA J  109  1                                  10    
HELIX  200 200 GLY J  110  MET J  115  5                                   6    
HELIX  201 201 PRO J  129  ARG J  134  1                                   6    
HELIX  202 202 PHE J  141  GLU J  151  1                                  11    
HELIX  203 203 SER J  169  ASN J  183  1                                  15    
HELIX  204 204 ARG J  201  GLY J  221  1                                  21    
HELIX  205 205 ASP J  233  LEU J  247  1                                  15    
HELIX  206 206 VAL J  256  GLY J  260  1                                   5    
HELIX  207 207 GLY J  260  TYR J  274  1                                  15    
HELIX  208 208 HIS J  285  ARG J  290  1                                   6    
HELIX  209 209 SER J  297  GLY J  309  1                                  13    
HELIX  210 210 GLU J  326  GLU J  339  1                                  14    
HELIX  211 211 ASN J  374  GLY J  383  1                                  10    
HELIX  212 212 GLY J  391  GLY J  396  1                                   6    
HELIX  213 213 GLY J  400  GLN J  417  1                                  18    
HELIX  214 214 PRO J  420  LYS J  426  1                                   7    
HELIX  215 215 HIS J  428  GLY J  439  1                                  12    
SHEET    1   A 5 LYS A  73  ASP A  79  0                                        
SHEET    2   A 5 TRP A  85  PRO A  92 -1  O  ALA A  90   N  LYS A  73           
SHEET    3   A 5 ASP A  24  PRO A  33 -1  N  ILE A  25   O  TYR A  91           
SHEET    4   A 5 VAL A 118  TYR A 127 -1  O  TYR A 127   N  ILE A  26           
SHEET    5   A 5 GLY A 295  ILE A 296  1  O  GLY A 295   N  LEU A 121           
SHEET    1   B 9 ILE A 157  VAL A 160  0                                        
SHEET    2   B 9 TYR A 187  KCX A 189  1  O  KCX A 189   N  VAL A 160           
SHEET    3   B 9 THR A 225  ASN A 229  1  O  PHE A 227   N  MET A 188           
SHEET    4   B 9 HIS A 251  ASP A 255  1  O  MET A 253   N  ALA A 228           
SHEET    5   B 9 ALA A 277  HIS A 281  1  O  HIS A 279   N  ALA A 252           
SHEET    6   B 9 GLN A 312  HIS A 314  1  O  GLN A 312   N  GLY A 280           
SHEET    7   B 9 PHE A 363  SER A 367  1  O  THR A 365   N  LEU A 313           
SHEET    8   B 9 VAL A 387  GLN A 389  1  O  VAL A 387   N  SER A 366           
SHEET    9   B 9 ILE A 157  VAL A 160  1  N  ILE A 157   O  LEU A 388           
SHEET    1   C 2 HIS A 341  TYR A 342  0                                        
SHEET    2   C 2 GLN A 354  LYS A 355 -1  O  GLN A 354   N  TYR A 342           
SHEET    1   D 5 LYS B  73  ASP B  79  0                                        
SHEET    2   D 5 TRP B  85  PRO B  92 -1  O  ILE B  86   N  HIS B  78           
SHEET    3   D 5 ASP B  24  PRO B  33 -1  N  PHE B  29   O  VAL B  87           
SHEET    4   D 5 VAL B 118  TYR B 127 -1  O  GLU B 124   N  VAL B  28           
SHEET    5   D 5 GLY B 295  ILE B 296  1  O  GLY B 295   N  LEU B 123           
SHEET    1   E 9 ILE B 157  VAL B 160  0                                        
SHEET    2   E 9 TYR B 187  KCX B 189  1  O  KCX B 189   N  VAL B 160           
SHEET    3   E 9 THR B 225  ASN B 229  1  O  PHE B 227   N  MET B 188           
SHEET    4   E 9 HIS B 251  ASP B 255  1  O  MET B 253   N  ALA B 228           
SHEET    5   E 9 ALA B 277  HIS B 281  1  O  HIS B 279   N  ALA B 252           
SHEET    6   E 9 GLN B 312  HIS B 314  1  O  GLN B 312   N  GLY B 280           
SHEET    7   E 9 PHE B 363  SER B 367  1  O  THR B 365   N  LEU B 313           
SHEET    8   E 9 VAL B 387  GLN B 389  1  O  VAL B 387   N  SER B 366           
SHEET    9   E 9 ILE B 157  VAL B 160  1  N  ILE B 157   O  LEU B 388           
SHEET    1   F 2 HIS B 341  TYR B 342  0                                        
SHEET    2   F 2 GLN B 354  LYS B 355 -1  O  GLN B 354   N  TYR B 342           
SHEET    1   G 5 LYS C  73  ASP C  79  0                                        
SHEET    2   G 5 TRP C  85  PRO C  92 -1  O  ILE C  86   N  HIS C  78           
SHEET    3   G 5 ASP C  24  PRO C  33 -1  N  ILE C  25   O  TYR C  91           
SHEET    4   G 5 VAL C 118  TYR C 127 -1  O  LYS C 119   N  THR C  32           
SHEET    5   G 5 GLY C 295  ILE C 296  1  O  GLY C 295   N  LEU C 123           
SHEET    1   H 9 ILE C 157  VAL C 160  0                                        
SHEET    2   H 9 TYR C 187  KCX C 189  1  O  KCX C 189   N  VAL C 160           
SHEET    3   H 9 THR C 225  ASN C 229  1  O  PHE C 227   N  MET C 188           
SHEET    4   H 9 HIS C 251  ASP C 255  1  O  MET C 253   N  ALA C 228           
SHEET    5   H 9 ALA C 277  HIS C 281  1  O  HIS C 281   N  VAL C 254           
SHEET    6   H 9 GLN C 312  HIS C 314  1  O  GLN C 312   N  GLY C 280           
SHEET    7   H 9 PHE C 363  SER C 367  1  O  THR C 365   N  LEU C 313           
SHEET    8   H 9 VAL C 387  GLN C 389  1  O  VAL C 387   N  SER C 366           
SHEET    9   H 9 ILE C 157  VAL C 160  1  N  ILE C 157   O  LEU C 388           
SHEET    1   I 2 HIS C 341  TYR C 342  0                                        
SHEET    2   I 2 GLN C 354  LYS C 355 -1  O  GLN C 354   N  TYR C 342           
SHEET    1   J 5 LYS D  73  ASP D  79  0                                        
SHEET    2   J 5 TRP D  85  PRO D  92 -1  O  ILE D  86   N  HIS D  78           
SHEET    3   J 5 ASP D  24  PRO D  33 -1  N  ILE D  25   O  TYR D  91           
SHEET    4   J 5 VAL D 118  TYR D 127 -1  O  LYS D 119   N  THR D  32           
SHEET    5   J 5 GLY D 295  ILE D 296  1  O  GLY D 295   N  LEU D 123           
SHEET    1   K 9 ILE D 157  VAL D 160  0                                        
SHEET    2   K 9 TYR D 187  KCX D 189  1  O  KCX D 189   N  VAL D 160           
SHEET    3   K 9 THR D 225  ASN D 229  1  O  PHE D 227   N  MET D 188           
SHEET    4   K 9 HIS D 251  ASP D 255  1  O  MET D 253   N  ALA D 228           
SHEET    5   K 9 ALA D 277  HIS D 281  1  O  HIS D 279   N  VAL D 254           
SHEET    6   K 9 GLN D 312  HIS D 314  1  O  GLN D 312   N  GLY D 280           
SHEET    7   K 9 PHE D 363  SER D 367  1  O  THR D 365   N  LEU D 313           
SHEET    8   K 9 VAL D 387  GLN D 389  1  O  VAL D 387   N  SER D 366           
SHEET    9   K 9 ILE D 157  VAL D 160  1  N  ILE D 157   O  LEU D 388           
SHEET    1   L 2 HIS D 341  TYR D 342  0                                        
SHEET    2   L 2 GLN D 354  LYS D 355 -1  O  GLN D 354   N  TYR D 342           
SHEET    1   M 5 LYS E  73  ASP E  79  0                                        
SHEET    2   M 5 TRP E  85  PRO E  92 -1  O  ILE E  86   N  HIS E  78           
SHEET    3   M 5 ASP E  24  PRO E  33 -1  N  ILE E  25   O  TYR E  91           
SHEET    4   M 5 VAL E 118  TYR E 127 -1  O  TYR E 127   N  ILE E  26           
SHEET    5   M 5 GLY E 295  ILE E 296  1  O  GLY E 295   N  LEU E 121           
SHEET    1   N 9 ILE E 157  VAL E 160  0                                        
SHEET    2   N 9 TYR E 187  KCX E 189  1  O  KCX E 189   N  VAL E 160           
SHEET    3   N 9 THR E 225  ASN E 229  1  O  PHE E 227   N  MET E 188           
SHEET    4   N 9 HIS E 251  ASP E 255  1  O  MET E 253   N  ALA E 228           
SHEET    5   N 9 ALA E 277  HIS E 281  1  O  ALA E 277   N  ALA E 252           
SHEET    6   N 9 GLN E 312  HIS E 314  1  O  GLN E 312   N  GLY E 280           
SHEET    7   N 9 PHE E 363  SER E 367  1  O  THR E 365   N  LEU E 313           
SHEET    8   N 9 VAL E 387  GLN E 389  1  O  VAL E 387   N  SER E 366           
SHEET    9   N 9 ILE E 157  VAL E 160  1  N  ILE E 157   O  LEU E 388           
SHEET    1   O 2 HIS E 341  TYR E 342  0                                        
SHEET    2   O 2 GLN E 354  LYS E 355 -1  O  GLN E 354   N  TYR E 342           
SHEET    1   P 5 LYS F  73  ASP F  79  0                                        
SHEET    2   P 5 TRP F  85  PRO F  92 -1  O  ALA F  90   N  LYS F  73           
SHEET    3   P 5 ASP F  24  PRO F  33 -1  N  ILE F  25   O  TYR F  91           
SHEET    4   P 5 VAL F 118  TYR F 127 -1  O  TYR F 127   N  ILE F  26           
SHEET    5   P 5 GLY F 295  ILE F 296  1  O  GLY F 295   N  LEU F 121           
SHEET    1   Q 9 ILE F 157  VAL F 160  0                                        
SHEET    2   Q 9 TYR F 187  KCX F 189  1  O  KCX F 189   N  VAL F 160           
SHEET    3   Q 9 THR F 225  ASN F 229  1  O  PHE F 227   N  MET F 188           
SHEET    4   Q 9 HIS F 251  ASP F 255  1  O  MET F 253   N  ALA F 228           
SHEET    5   Q 9 ALA F 277  HIS F 281  1  O  HIS F 281   N  VAL F 254           
SHEET    6   Q 9 GLN F 312  HIS F 314  1  O  GLN F 312   N  GLY F 280           
SHEET    7   Q 9 PHE F 363  SER F 367  1  O  THR F 365   N  LEU F 313           
SHEET    8   Q 9 VAL F 387  GLN F 389  1  O  VAL F 387   N  SER F 366           
SHEET    9   Q 9 ILE F 157  VAL F 160  1  N  ILE F 157   O  LEU F 388           
SHEET    1   R 2 HIS F 341  TYR F 342  0                                        
SHEET    2   R 2 GLN F 354  LYS F 355 -1  O  GLN F 354   N  TYR F 342           
SHEET    1   S 5 LYS G  73  ASP G  79  0                                        
SHEET    2   S 5 TRP G  85  PRO G  92 -1  O  ILE G  86   N  HIS G  78           
SHEET    3   S 5 ASP G  24  PRO G  33 -1  N  ILE G  25   O  TYR G  91           
SHEET    4   S 5 VAL G 118  TYR G 127 -1  O  LYS G 119   N  THR G  32           
SHEET    5   S 5 GLY G 295  ILE G 296  1  O  GLY G 295   N  LEU G 123           
SHEET    1   T 9 ILE G 157  VAL G 160  0                                        
SHEET    2   T 9 TYR G 187  KCX G 189  1  O  KCX G 189   N  VAL G 160           
SHEET    3   T 9 THR G 225  ASN G 229  1  O  PHE G 227   N  MET G 188           
SHEET    4   T 9 HIS G 251  ASP G 255  1  O  MET G 253   N  ALA G 228           
SHEET    5   T 9 ALA G 277  HIS G 281  1  O  HIS G 281   N  VAL G 254           
SHEET    6   T 9 GLN G 312  HIS G 314  1  O  GLN G 312   N  GLY G 280           
SHEET    7   T 9 PHE G 363  SER G 367  1  O  THR G 365   N  LEU G 313           
SHEET    8   T 9 VAL G 387  GLN G 389  1  O  VAL G 387   N  SER G 366           
SHEET    9   T 9 ILE G 157  VAL G 160  1  N  ILE G 157   O  LEU G 388           
SHEET    1   U 2 HIS G 341  TYR G 342  0                                        
SHEET    2   U 2 GLN G 354  LYS G 355 -1  O  GLN G 354   N  TYR G 342           
SHEET    1   V 5 LYS H  73  ASP H  79  0                                        
SHEET    2   V 5 TRP H  85  PRO H  92 -1  O  ILE H  86   N  HIS H  78           
SHEET    3   V 5 ASP H  24  PRO H  33 -1  N  ILE H  25   O  TYR H  91           
SHEET    4   V 5 VAL H 118  TYR H 127 -1  O  TYR H 127   N  ILE H  26           
SHEET    5   V 5 GLY H 295  ILE H 296  1  O  GLY H 295   N  LEU H 121           
SHEET    1   W 9 ILE H 157  VAL H 160  0                                        
SHEET    2   W 9 TYR H 187  KCX H 189  1  O  KCX H 189   N  VAL H 160           
SHEET    3   W 9 THR H 225  ASN H 229  1  O  PHE H 227   N  MET H 188           
SHEET    4   W 9 HIS H 251  ASP H 255  1  O  MET H 253   N  ALA H 228           
SHEET    5   W 9 ALA H 277  HIS H 281  1  O  HIS H 281   N  VAL H 254           
SHEET    6   W 9 GLN H 312  HIS H 314  1  O  GLN H 312   N  GLY H 280           
SHEET    7   W 9 PHE H 363  SER H 367  1  O  THR H 365   N  LEU H 313           
SHEET    8   W 9 VAL H 387  GLN H 389  1  O  VAL H 387   N  PRO H 364           
SHEET    9   W 9 ILE H 157  VAL H 160  1  N  ILE H 157   O  LEU H 388           
SHEET    1   X 2 HIS H 341  TYR H 342  0                                        
SHEET    2   X 2 GLN H 354  LYS H 355 -1  O  GLN H 354   N  TYR H 342           
SHEET    1   Y 5 LYS I  73  ASP I  79  0                                        
SHEET    2   Y 5 TRP I  85  PRO I  92 -1  O  ALA I  90   N  LYS I  73           
SHEET    3   Y 5 ASP I  24  PRO I  33 -1  N  VAL I  31   O  TRP I  85           
SHEET    4   Y 5 VAL I 118  TYR I 127 -1  O  LYS I 119   N  THR I  32           
SHEET    5   Y 5 GLY I 295  ILE I 296  1  O  GLY I 295   N  LEU I 121           
SHEET    1   Z 9 ILE I 157  VAL I 160  0                                        
SHEET    2   Z 9 TYR I 187  KCX I 189  1  O  KCX I 189   N  VAL I 160           
SHEET    3   Z 9 THR I 225  ASN I 229  1  O  PHE I 227   N  MET I 188           
SHEET    4   Z 9 HIS I 251  ASP I 255  1  O  MET I 253   N  ALA I 228           
SHEET    5   Z 9 ALA I 277  HIS I 281  1  O  HIS I 279   N  ALA I 252           
SHEET    6   Z 9 GLN I 312  HIS I 314  1  O  GLN I 312   N  GLY I 280           
SHEET    7   Z 9 PHE I 363  SER I 367  1  O  THR I 365   N  LEU I 313           
SHEET    8   Z 9 VAL I 387  GLN I 389  1  O  VAL I 387   N  SER I 366           
SHEET    9   Z 9 ILE I 157  VAL I 160  1  N  ILE I 157   O  LEU I 388           
SHEET    1  AA 2 HIS I 341  TYR I 342  0                                        
SHEET    2  AA 2 GLN I 354  LYS I 355 -1  O  GLN I 354   N  TYR I 342           
SHEET    1  AB 5 LYS J  73  ASP J  79  0                                        
SHEET    2  AB 5 TRP J  85  PRO J  92 -1  O  ILE J  86   N  HIS J  78           
SHEET    3  AB 5 ASP J  24  PRO J  33 -1  N  ILE J  25   O  TYR J  91           
SHEET    4  AB 5 VAL J 118  TYR J 127 -1  O  LYS J 119   N  THR J  32           
SHEET    5  AB 5 GLY J 295  ILE J 296  1  O  GLY J 295   N  LEU J 121           
SHEET    1  AC 9 ILE J 157  VAL J 160  0                                        
SHEET    2  AC 9 TYR J 187  KCX J 189  1  O  KCX J 189   N  VAL J 160           
SHEET    3  AC 9 THR J 225  ASN J 229  1  O  PHE J 227   N  MET J 188           
SHEET    4  AC 9 HIS J 251  ASP J 255  1  O  MET J 253   N  ALA J 228           
SHEET    5  AC 9 ALA J 277  HIS J 281  1  O  HIS J 281   N  VAL J 254           
SHEET    6  AC 9 GLN J 312  HIS J 314  1  O  GLN J 312   N  GLY J 280           
SHEET    7  AC 9 PHE J 363  SER J 367  1  O  PHE J 363   N  LEU J 313           
SHEET    8  AC 9 VAL J 387  GLN J 389  1  O  VAL J 387   N  SER J 366           
SHEET    9  AC 9 ILE J 157  VAL J 160  1  N  ILE J 157   O  LEU J 388           
SHEET    1  AD 2 HIS J 341  TYR J 342  0                                        
SHEET    2  AD 2 GLN J 354  LYS J 355 -1  O  GLN J 354   N  TYR J 342           
LINK         C   MET A 188                 N   KCX A 189     1555   1555  1.33  
LINK         C   KCX A 189                 N   ASP A 190     1555   1555  1.33  
LINK         C   MET B 188                 N   KCX B 189     1555   1555  1.33  
LINK         C   KCX B 189                 N   ASP B 190     1555   1555  1.33  
LINK         C   MET C 188                 N   KCX C 189     1555   1555  1.33  
LINK         C   KCX C 189                 N   ASP C 190     1555   1555  1.33  
LINK         C   MET D 188                 N   KCX D 189     1555   1555  1.33  
LINK         C   KCX D 189                 N   ASP D 190     1555   1555  1.33  
LINK         C   MET E 188                 N   KCX E 189     1555   1555  1.33  
LINK         C   KCX E 189                 N   ASP E 190     1555   1555  1.33  
LINK         C   MET F 188                 N   KCX F 189     1555   1555  1.33  
LINK         C   KCX F 189                 N   ASP F 190     1555   1555  1.33  
LINK         C   MET G 188                 N   KCX G 189     1555   1555  1.33  
LINK         C   KCX G 189                 N   ASP G 190     1555   1555  1.33  
LINK         C   MET H 188                 N   KCX H 189     1555   1555  1.33  
LINK         C   KCX H 189                 N   ASP H 190     1555   1555  1.33  
LINK         C   MET I 188                 N   KCX I 189     1555   1555  1.33  
LINK         C   KCX I 189                 N   ASP I 190     1555   1555  1.33  
LINK         C   MET J 188                 N   KCX J 189     1555   1555  1.33  
LINK         C   KCX J 189                 N   ASP J 190     1555   1555  1.33  
LINK         OQ2 KCX A 189                MG    MG A 500     1555   1555  1.96  
LINK         OD1 ASP A 191                MG    MG A 500     1555   1555  2.07  
LINK         OE1 GLU A 192                MG    MG A 500     1555   1555  1.82  
LINK         OQ2 KCX B 189                MG    MG B 500     1555   1555  1.98  
LINK         OD1 ASP B 191                MG    MG B 500     1555   1555  2.05  
LINK         OE1 GLU B 192                MG    MG B 500     1555   1555  2.04  
LINK         OQ2 KCX C 189                MG    MG C 500     1555   1555  1.93  
LINK         OD1 ASP C 191                MG    MG C 500     1555   1555  2.03  
LINK         OE1 GLU C 192                MG    MG C 500     1555   1555  2.03  
LINK         OQ2 KCX D 189                MG    MG D 500     1555   1555  1.90  
LINK         OD1 ASP D 191                MG    MG D 500     1555   1555  1.90  
LINK         OE1 GLU D 192                MG    MG D 500     1555   1555  1.99  
LINK         OQ2 KCX E 189                MG    MG E 500     1555   1555  2.06  
LINK         OD1 ASP E 191                MG    MG E 500     1555   1555  1.99  
LINK         OE1 GLU E 192                MG    MG E 500     1555   1555  2.10  
LINK         OQ2 KCX F 189                MG    MG F 500     1555   1555  1.99  
LINK         OD1 ASP F 191                MG    MG F 500     1555   1555  1.93  
LINK         OE1 GLU F 192                MG    MG F 500     1555   1555  2.04  
LINK         OQ2 KCX G 189                MG    MG G 500     1555   1555  2.02  
LINK         OD1 ASP G 191                MG    MG G 500     1555   1555  2.00  
LINK         OE1 GLU G 192                MG    MG G 500     1555   1555  1.91  
LINK         OQ2 KCX H 189                MG    MG H 500     1555   1555  2.08  
LINK         OE1 GLU H 192                MG    MG H 500     1555   1555  1.97  
LINK         OQ2 KCX I 189                MG    MG I 500     1555   1555  1.94  
LINK         OD1 ASP I 191                MG    MG I 500     1555   1555  2.03  
LINK         OE1 GLU I 192                MG    MG I 500     1555   1555  2.08  
LINK         OQ2 KCX J 189                MG    MG J 500     1555   1555  2.05  
LINK         OD2 ASP J 191                MG    MG J 500     1555   1555  1.99  
LINK         OE1 GLU J 192                MG    MG J 500     1555   1555  2.09  
LINK        MG    MG A 500                 O3  CAP A 600     1555   1555  2.10  
LINK        MG    MG A 500                 O2  CAP A 600     1555   1555  2.26  
LINK        MG    MG A 500                 O7  CAP A 600     1555   1555  2.30  
LINK        MG    MG B 500                 O3  CAP B 600     1555   1555  2.21  
LINK        MG    MG B 500                 O7  CAP B 600     1555   1555  2.11  
LINK        MG    MG B 500                 O2  CAP B 600     1555   1555  2.23  
LINK        MG    MG C 500                 O2  CAP C 600     1555   1555  2.38  
LINK        MG    MG C 500                 O7  CAP C 600     1555   1555  2.00  
LINK        MG    MG C 500                 O3  CAP C 600     1555   1555  2.17  
LINK        MG    MG D 500                 O3  CAP D 600     1555   1555  2.09  
LINK        MG    MG D 500                 O2  CAP D 600     1555   1555  2.36  
LINK        MG    MG D 500                 O7  CAP D 600     1555   1555  2.08  
LINK        MG    MG E 500                 O3  CAP E 600     1555   1555  2.07  
LINK        MG    MG E 500                 O2  CAP E 600     1555   1555  2.27  
LINK        MG    MG E 500                 O7  CAP E 600     1555   1555  1.89  
LINK        MG    MG F 500                 O3  CAP F 600     1555   1555  2.09  
LINK        MG    MG F 500                 O2  CAP F 600     1555   1555  2.39  
LINK        MG    MG F 500                 O7  CAP F 600     1555   1555  2.01  
LINK        MG    MG G 500                 O3  CAP G 600     1555   1555  2.07  
LINK        MG    MG G 500                 O7  CAP G 600     1555   1555  1.98  
LINK        MG    MG G 500                 O2  CAP G 600     1555   1555  2.33  
LINK        MG    MG H 500                 O2  CAP H 600     1555   1555  2.34  
LINK        MG    MG H 500                 O7  CAP H 600     1555   1555  2.21  
LINK        MG    MG H 500                 O3  CAP H 600     1555   1555  2.17  
LINK        MG    MG I 500                 O2  CAP I 600     1555   1555  2.29  
LINK        MG    MG I 500                 O3  CAP I 600     1555   1555  2.10  
LINK        MG    MG I 500                 O7  CAP I 600     1555   1555  2.19  
LINK        MG    MG J 500                 O3  CAP J 600     1555   1555  2.19  
LINK        MG    MG J 500                 O2  CAP J 600     1555   1555  2.24  
LINK        MG    MG J 500                 O7  CAP J 600     1555   1555  1.90  
LINK         OD2 ASP H 191                MG    MG H 500     1555   1555  2.66  
CISPEP   1 LYS A  163    PRO A  164          0         5.99                     
CISPEP   2 LYS B  163    PRO B  164          0         6.80                     
CISPEP   3 LYS C  163    PRO C  164          0         6.37                     
CISPEP   4 LYS D  163    PRO D  164          0         8.12                     
CISPEP   5 LYS E  163    PRO E  164          0         5.64                     
CISPEP   6 LYS F  163    PRO F  164          0         6.30                     
CISPEP   7 LYS G  163    PRO G  164          0         5.38                     
CISPEP   8 LYS H  163    PRO H  164          0         6.42                     
CISPEP   9 LYS I  163    PRO I  164          0         6.65                     
CISPEP  10 LYS J  163    PRO J  164          0         5.79                     
SITE     1 AC1  6 LYS A 165  KCX A 189  ASP A 191  GLU A 192                    
SITE     2 AC1  6 CAP A 600  ASN H 111                                          
SITE     1 AC2 26 VAL A 161  LYS A 163  LYS A 165  KCX A 189                    
SITE     2 AC2 26 ASP A 191  GLU A 192  HIS A 281  ARG A 282                    
SITE     3 AC2 26 HIS A 314  LYS A 322  LEU A 323  SER A 367                    
SITE     4 AC2 26 GLY A 368  GLY A 369  GLN A 389  GLY A 391                    
SITE     5 AC2 26 GLY A 392  HOH A 495   MG A 500  HOH A 645                    
SITE     6 AC2 26 HOH A1278  HOH A1893  HOH A2850  THR H  54                    
SITE     7 AC2 26 TRP H  55  ASN H 111                                          
SITE     1 AC3  4 KCX B 189  ASP B 191  GLU B 192  CAP B 600                    
SITE     1 AC4 28 LYS B 163  LYS B 165  KCX B 189  ASP B 191                    
SITE     2 AC4 28 GLU B 192  HIS B 281  ARG B 282  HIS B 314                    
SITE     3 AC4 28 LYS B 322  LEU B 323  SER B 367  GLY B 368                    
SITE     4 AC4 28 GLY B 369  GLN B 389  GLY B 391  GLY B 392                    
SITE     5 AC4 28 HOH B 467  HOH B 468  HOH B 472  HOH B 499                    
SITE     6 AC4 28  MG B 500  HOH B2398  HOH B2720  HOH B2839                    
SITE     7 AC4 28 GLU G  49  TRP G  55  ASN G 111  HOH G 466                    
SITE     1 AC5  5 KCX C 189  ASP C 191  GLU C 192  CAP C 600                    
SITE     2 AC5  5 ASN F 111                                                     
SITE     1 AC6 29 LYS C 163  LYS C 165  KCX C 189  ASP C 191                    
SITE     2 AC6 29 GLU C 192  HIS C 281  ARG C 282  HIS C 314                    
SITE     3 AC6 29 LYS C 322  LEU C 323  SER C 367  GLY C 368                    
SITE     4 AC6 29 GLY C 369  GLN C 389  GLY C 391  GLY C 392                    
SITE     5 AC6 29 HOH C 445  HOH C 457  HOH C 461  HOH C 487                    
SITE     6 AC6 29  MG C 500  HOH C 616  HOH C 691  HOH C2321                    
SITE     7 AC6 29 GLU F  49  TRP F  55  ASN F 111  HOH F 503                    
SITE     8 AC6 29 HOH F1009                                                     
SITE     1 AC7  4 KCX D 189  ASP D 191  GLU D 192  CAP D 600                    
SITE     1 AC8 28 LYS D 163  LYS D 165  KCX D 189  ASP D 191                    
SITE     2 AC8 28 GLU D 192  HIS D 281  ARG D 282  HIS D 314                    
SITE     3 AC8 28 LYS D 322  LEU D 323  SER D 367  GLY D 368                    
SITE     4 AC8 28 GLY D 369  GLN D 389  GLY D 391  GLY D 392                    
SITE     5 AC8 28 HOH D 445  HOH D 452  HOH D 458   MG D 500                    
SITE     6 AC8 28 HOH D 510  HOH D1721  HOH D2695  HOH D2855                    
SITE     7 AC8 28 GLU J  49  TRP J  55  ASN J 111  HOH J2762                    
SITE     1 AC9  4 KCX E 189  ASP E 191  GLU E 192  CAP E 600                    
SITE     1 BC1 28 LYS E 163  LYS E 165  KCX E 189  ASP E 191                    
SITE     2 BC1 28 GLU E 192  HIS E 281  ARG E 282  HIS E 314                    
SITE     3 BC1 28 LYS E 322  LEU E 323  SER E 367  GLY E 368                    
SITE     4 BC1 28 GLY E 369  GLN E 389  GLY E 391  GLY E 392                    
SITE     5 BC1 28 HOH E 483  HOH E 494   MG E 500  HOH E 654                    
SITE     6 BC1 28 HOH E 676  HOH E1879  HOH E2240  GLU I  49                    
SITE     7 BC1 28 TRP I  55  ASN I 111  HOH I 463  HOH I 465                    
SITE     1 BC2  5 ASN C 111  KCX F 189  ASP F 191  GLU F 192                    
SITE     2 BC2  5 CAP F 600                                                     
SITE     1 BC3 28 GLU C  49  THR C  54  TRP C  55  ASN C 111                    
SITE     2 BC3 28 HOH C 451  HOH C 478  LYS F 163  LYS F 165                    
SITE     3 BC3 28 KCX F 189  ASP F 191  GLU F 192  HIS F 281                    
SITE     4 BC3 28 ARG F 282  HIS F 314  LYS F 322  LEU F 323                    
SITE     5 BC3 28 SER F 367  GLY F 368  GLY F 369  GLN F 389                    
SITE     6 BC3 28 GLY F 391  GLY F 392  HOH F 445  HOH F 464                    
SITE     7 BC3 28 HOH F 490  HOH F 495  HOH F 498   MG F 500                    
SITE     1 BC4  5 ASN B 111  KCX G 189  ASP G 191  GLU G 192                    
SITE     2 BC4  5 CAP G 600                                                     
SITE     1 BC5 28 GLU B  49  TRP B  55  ASN B 111  HOH B 448                    
SITE     2 BC5 28 HOH B 454  LYS G 163  LYS G 165  KCX G 189                    
SITE     3 BC5 28 ASP G 191  GLU G 192  HIS G 281  ARG G 282                    
SITE     4 BC5 28 HIS G 314  LYS G 322  LEU G 323  SER G 367                    
SITE     5 BC5 28 GLY G 368  GLY G 369  GLN G 389  GLY G 391                    
SITE     6 BC5 28 GLY G 392  HOH G 446  HOH G 456  HOH G 469                    
SITE     7 BC5 28 HOH G 485   MG G 500  HOH G 530  HOH G1761                    
SITE     1 BC6  4 KCX H 189  ASP H 191  GLU H 192  CAP H 600                    
SITE     1 BC7 25 TRP A  55  ASN A 111  HOH A1659  LYS H 163                    
SITE     2 BC7 25 LYS H 165  KCX H 189  ASP H 191  GLU H 192                    
SITE     3 BC7 25 HIS H 281  ARG H 282  HIS H 314  LYS H 322                    
SITE     4 BC7 25 LEU H 323  SER H 367  GLY H 368  GLY H 369                    
SITE     5 BC7 25 GLN H 389  GLY H 391  GLY H 392  HOH H 457                    
SITE     6 BC7 25  MG H 500  HOH H1169  HOH H1230  HOH H2657                    
SITE     7 BC7 25 HOH H2710                                                     
SITE     1 BC8  4 KCX I 189  ASP I 191  GLU I 192  CAP I 600                    
SITE     1 BC9 28 GLU E  49  TRP E  55  ASN E 111  HOH E 505                    
SITE     2 BC9 28 LYS I 163  LYS I 165  KCX I 189  ASP I 191                    
SITE     3 BC9 28 GLU I 192  HIS I 281  ARG I 282  HIS I 314                    
SITE     4 BC9 28 LYS I 322  LEU I 323  SER I 367  GLY I 368                    
SITE     5 BC9 28 GLY I 369  GLN I 389  GLY I 391  GLY I 392                    
SITE     6 BC9 28 HOH I 445  HOH I 451  HOH I 471  HOH I 478                    
SITE     7 BC9 28 HOH I 482  HOH I 483  HOH I 491   MG I 500                    
SITE     1 CC1  5 ASN D 111  KCX J 189  ASP J 191  GLU J 192                    
SITE     2 CC1  5 CAP J 600                                                     
SITE     1 CC2 28 GLU D  49  TRP D  55  ASN D 111  HOH D 482                    
SITE     2 CC2 28 HOH D 484  LYS J 163  LYS J 165  KCX J 189                    
SITE     3 CC2 28 ASP J 191  GLU J 192  HIS J 281  ARG J 282                    
SITE     4 CC2 28 HIS J 314  LYS J 322  LEU J 323  SER J 367                    
SITE     5 CC2 28 GLY J 368  GLY J 369  GLN J 389  GLY J 391                    
SITE     6 CC2 28 GLY J 392  HOH J 445  HOH J 481   MG J 500                    
SITE     7 CC2 28 HOH J 578  HOH J 602  HOH J1892  HOH J1895                    
CRYST1   97.474  246.241  133.080  90.00 104.10  90.00 P 1 21 1     20          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010259  0.000000  0.002577        0.00000                         
SCALE2      0.000000  0.004061  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007748        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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